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Protein

Periplakin

Gene

Ppl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Keratinization

Names & Taxonomyi

Protein namesi
Recommended name:
Periplakin
Gene namesi
Name:Ppl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1194898. Ppl.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • desmosome Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • extrinsic component of plasma membrane Source: MGI
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17551755PeriplakinPRO_0000078150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei463 – 4631PhosphoserineBy similarity
Modified residuei885 – 8851PhosphoserineBy similarity
Modified residuei947 – 9471PhosphoserineBy similarity
Modified residuei1583 – 15831PhosphoserineBy similarity
Modified residuei1656 – 16561PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9R269.
PaxDbiQ9R269.
PRIDEiQ9R269.

PTM databases

iPTMnetiQ9R269.
PhosphoSiteiQ9R269.

Expressioni

Tissue specificityi

Upper granular cell layer of dorsal lip and tongue, palate and dorsal epidermis.1 Publication

Gene expression databases

CleanExiMM_PPL.

Interactioni

Subunit structurei

Homodimer or a heterodimer with EVPL. Interacts with PPHLN1 and VIM. Binds to the PH domain of AKT1. Interacts with FCGR1A (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1Q013142EBI-368293,EBI-368344From a different organism.
VimP201522EBI-368293,EBI-299269

Protein-protein interaction databases

BioGridi202331. 5 interactions.
IntActiQ9R269. 5 interactions.
MINTiMINT-4998469.
STRINGi10090.ENSMUSP00000039360.

Structurei

3D structure databases

ProteinModelPortaliQ9R269.
SMRiQ9R269. Positions 1653-1753.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati214 – 315102Spectrin 1Add
BLAST
Repeati321 – 483163Spectrin 2Add
BLAST
Repeati503 – 610108Spectrin 3Add
BLAST
Repeati1650 – 168435Plectin 1Add
BLAST
Repeati1699 – 173436Plectin 2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili16 – 125110Sequence analysisAdd
BLAST
Coiled coili182 – 387206Sequence analysisAdd
BLAST
Coiled coili611 – 819209Sequence analysisAdd
BLAST
Coiled coili883 – 1644762Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the plakin or cytolinker family.Curated
Contains 2 plectin repeats.Curated
Contains 3 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IQBN. Eukaryota.
ENOG410YHVZ. LUCA.
HOGENOMiHOG000168302.
HOVERGENiHBG053564.
InParanoidiQ9R269.
KOiK10386.
PhylomeDBiQ9R269.

Family and domain databases

InterProiIPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
SMARTiSM00250. PLEC. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMiSSF75399. SSF75399. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9R269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSLFRKRNK GKYSPTVQTR SISNKELSDL IEQLQKNADQ VERNIVDTEA
60 70 80 90 100
KMQSDLARMQ EGQLPEHRDA ALQNVSDSEK LLYVLEADSA IAKHMKHPQG
110 120 130 140 150
DMIAEDIRQL KERVTNLRGK HKQMYSLAVK EADPRVNWDT LVDEKLDKLS
160 170 180 190 200
SQSFGTDLPL VDSQVEQHNI FHNEVKAIGP HLAKDKEQNS ELQAKYQKLL
210 220 230 240 250
TASQARQQHL SSLQDYMQRC TNELYWLDQQ AKGRMQYDWS DRNLDYPSRR
260 270 280 290 300
RQYENFINRN LEAKEERINK LHTEGDQLLT AEHPGRNSIE AHMEAVHAEW
310 320 330 340 350
KEYLNLLICE ESHLKYMEDY HQFHKDMKDA QELLRKVDSD LNQKYSPDFK
360 370 380 390 400
DRYQIELLLR ELDDQEKALD KYEDVVRGLQ RRGQQVVPLK YRRETPLKPI
410 420 430 440 450
PVEALCDFES DQGLISRGYS YTLQKNNGES WELTDSTGKK LAAPAVCFII
460 470 480 490 500
PPTDPEALAL ADSLGSQYRS VRQKATGSKH ALQQRHEVLR TENPGDASDL
510 520 530 540 550
QGRQLLAGLD KVASDLDRQE KAITGILRPP LEQGRAIEDS AERAKGLKNI
560 570 580 590 600
TNELLQIEPE KTQCTAECEA FVQALPASGT APLLKTRVED TNQKYERLVW
610 620 630 640 650
LLEAAQEKVD VANRLENSLQ RGRELLASYE NRLIQDDTMP ESGHVLDRKR
660 670 680 690 700
QELEAMASEL QAHKSLLGEV GKNLQVAKQC SSSLASRFQE HCPDLERQEA
710 720 730 740 750
EVHKLNQRFN NLSQQVERRA QSLQSARAAY DEYCSGYNRV LQFLAKTPSY
760 770 780 790 800
EPQETDSLGQ METKLKNQKN LLDELASREQ EVQKVYADSQ QYQQAVKDYE
810 820 830 840 850
LEAEKLRSLL DLENGRNSHV NKRARLQSPA AKVKEEEAAL AAKFTEVNAI
860 870 880 890 900
NRQRLQNLEF ALNLLRQQPE AGVTHETLQG GKLSSGMEET WKIKKELEEE
910 920 930 940 950
IERRQQLENE VKSAQEEIQT LKDQGPQESL VRKEVLKKVP DPALEESFQQ
960 970 980 990 1000
LQQTLAEEQH KNQLLQEELG ALQLRLQALE QETRDGGQEY VVKEVLRIEP
1010 1020 1030 1040 1050
DRAQEDEVLQ LREELEALRR QKGAREAEVL LLQQRVAALA AEKSRVQEKV
1060 1070 1080 1090 1100
TEREVVKLQN DPQLEAEYRR LQEEHQREGT LREKQEEELS FLQAKLRRLE
1110 1120 1130 1140 1150
KERAMAEGKI TVKEVLKVEK DAAVEREVND LTRQYEDEAA KARSGQREKT
1160 1170 1180 1190 1200
ELLRKIWALE EENAKVVVQE KVREIVRPDP KAESEVANLR LELVEQERKF
1210 1220 1230 1240 1250
RGAEEQLKSY QSELEALRNR GPQVEVKEVT KEVIKYTTDP ETEQELQRLR
1260 1270 1280 1290 1300
EEIMDKTRLI ERCDLEIYQL KQEIQALKDT KPQVQTREVV QEILQFQEDP
1310 1320 1330 1340 1350
QTKKEVESLR IQLSEEQKKQ VDLEGERASQ EEKIKRKEEE LAQQRKERVV
1360 1370 1380 1390 1400
RQEVVQYEDE PDLRAEVTAF TNSIDAELRQ IDKLHVELRR LQHRRAELER
1410 1420 1430 1440 1450
QLEELERERQ ARRAAELEVQ RLQQRLAALE QEEAKTGEKV THTQKVVLQQ
1460 1470 1480 1490 1500
DPQQTREHAL LRAQLEEERH RRQLLEGELE PLRRKLAALE KAEIKEKVVF
1510 1520 1530 1540 1550
SESVQVEKGD TEQEIQRLKK SLEEESQSKR ELDSEVTRLE AKLSELEFYN
1560 1570 1580 1590 1600
SKSSKELDFL REENHKLQLE RQNLQLETRR LQSEIEMAAT ETRDLKNITT
1610 1620 1630 1640 1650
IDSGTHLNSR LWSLEKELDD LKKMSKDKDL EIDELQRRLG SVAVKREQRE
1660 1670 1680 1690 1700
NHLRRSIVVI DPDTGRELSP EEAHRAGLID WKMFVKLRSQ ECDWEEISVK
1710 1720 1730 1740 1750
GPNGESSVIH DRKSGKKFSI EDALQSGRLT AAQYDRYVNK DMSIQELAVL

VSGQK
Length:1,755
Mass (Da):204,004
Last modified:May 1, 2000 - v1
Checksum:i3FEA343086E4CB8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661E → Q in AAF29436 (PubMed:15226441).Curated
Sequence conflicti592 – 5921N → T in AAF29436 (PubMed:15226441).Curated
Sequence conflicti648 – 6481R → S in AAF29436 (PubMed:15226441).Curated
Sequence conflicti671 – 6722GK → EQ in AAF29436 (PubMed:15226441).Curated
Sequence conflicti983 – 9831T → A in AAF29436 (PubMed:15226441).Curated
Sequence conflicti1325 – 13251G → R in AAF29436 (PubMed:15226441).Curated
Sequence conflicti1344 – 13452QR → G in AAF29436 (PubMed:15226441).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126834 mRNA. Translation: AAD20642.1.
AF116523
, AF116519, AF116520, AF116521, AF116522 Genomic DNA. Translation: AAF29436.2.
AK014700 mRNA. Translation: BAB29510.1.
AF013715 Genomic DNA. Translation: AAC40068.1.
RefSeqiNP_032935.2. NM_008909.2.
UniGeneiMm.266875.

Genome annotation databases

GeneIDi19041.
KEGGimmu:19041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126834 mRNA. Translation: AAD20642.1.
AF116523
, AF116519, AF116520, AF116521, AF116522 Genomic DNA. Translation: AAF29436.2.
AK014700 mRNA. Translation: BAB29510.1.
AF013715 Genomic DNA. Translation: AAC40068.1.
RefSeqiNP_032935.2. NM_008909.2.
UniGeneiMm.266875.

3D structure databases

ProteinModelPortaliQ9R269.
SMRiQ9R269. Positions 1653-1753.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202331. 5 interactions.
IntActiQ9R269. 5 interactions.
MINTiMINT-4998469.
STRINGi10090.ENSMUSP00000039360.

PTM databases

iPTMnetiQ9R269.
PhosphoSiteiQ9R269.

Proteomic databases

MaxQBiQ9R269.
PaxDbiQ9R269.
PRIDEiQ9R269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi19041.
KEGGimmu:19041.

Organism-specific databases

CTDi5493.
MGIiMGI:1194898. Ppl.

Phylogenomic databases

eggNOGiENOG410IQBN. Eukaryota.
ENOG410YHVZ. LUCA.
HOGENOMiHOG000168302.
HOVERGENiHBG053564.
InParanoidiQ9R269.
KOiK10386.
PhylomeDBiQ9R269.

Miscellaneous databases

ChiTaRSiPpl. mouse.
PROiQ9R269.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PPL.

Family and domain databases

InterProiIPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
SMARTiSM00250. PLEC. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMiSSF75399. SSF75399. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH AKT1 AND VIM.
    Tissue: Embryo.
  2. "Periplakin gene targeting reveals a constituent of the cornified cell envelope dispensable for normal mouse development."
    Aho S., Li K., Ryoo Y., McGee C., Ishida-Yamamoto A., Uitto J., Klement J.F.
    Mol. Cell. Biol. 24:6410-6418(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: 129/Sv.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1643-1755.
    Strain: C57BL/6J.
    Tissue: Head.
  4. "cDNA cloning, mRNA expression, and chromosomal mapping of human and mouse periplakin genes."
    Aho S., McLean W.H.I., Li K., Uitto J.
    Genomics 48:242-247(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1647-1755.
    Strain: C57BL/6J.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Lung.

Entry informationi

Entry nameiPEPL_MOUSE
AccessioniPrimary (citable) accession number: Q9R269
Secondary accession number(s): O70231, Q9CUT1, Q9JLZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.